Metabolism Part 3 - Protein

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Oct 30, 2023

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Protein 1
2 What’s on the Menu! Some protein basics: turnover, changes with exercise. The practical stuff: how much? protein type coingestion with carbs timing of ingestion changes with training status changes with aging
Protein Turnover and the Various Metabolic Fates of AAs in Skeletal Muscle During post-absorptive state, breakdown is generally ~30% greater than synthesis A protein rich meal increases synthesis and decreases breakdown During prolonged exercise, • increase in protein breakdown and decrease in synthesis • Small increase in oxidation ( only 2 - 6% of total energy) 3 Note that during protein turnover, amino acids are recycled … this explains why daily need aren’t as high as you might expect
Amino Acids Essential amino acids • cannot be produced by the body in physiologically significant amounts Non-essential • can be produced by the body Branched-chain • leucine*, isoleucine, valine • only AAs oxidized by muscle *potent stimulator of protein synthesis 4 Essential AA’s Leucine Isoleucine Valine Methionine Phenylalanine Threonine Lysine Histidine Tryptophan
Fates of Amino Acids During Exercise Urea production • All oxidized AAs will lead to urea production • Urea is excreted, ↑ with exercise, especially carbohydrate-depleted situations (i.e. greater dependency on AA) Branched chain amino acids (BCAAs, leucine, isoleucine, valine) • Major group of AAs that are oxidized in muscle • Oxidation of BCAAs increases with exercise – Generally not a significant substrate for muscle ATP production Gluconeogenic, ketogenic or oxidized • Glucogenic AAs readily converted to pyruvate, or TCA intermediate e.g. (ketoglutarate, succinate, fumarate); many amino acids are gluconeogenic • Ketogenic AAs readily converted to acetyl-CoA or acetoacetate; leucine, alanine and a few others • Most can be oxidized; in muscle, mainly BCAAs 5
6 What About Resistance Exercise? Tom Platz! 1980s bodybuilder
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